R
Ri Yao Yang
Researcher at University of Texas MD Anderson Cancer Center
Publications - 36
Citations - 3932
Ri Yao Yang is an academic researcher from University of Texas MD Anderson Cancer Center. The author has contributed to research in topics: Galectin & Immunotherapy. The author has an hindex of 20, co-authored 33 publications receiving 3358 citations. Previous affiliations of Ri Yao Yang include Scripps Research Institute & La Jolla Institute for Allergy and Immunology.
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Journal ArticleDOI
Galectin-9 interacts with PD-1 and TIM-3 to regulate T cell death and is a target for cancer immunotherapy.
Ri Yao Yang,Linlin Sun,Linlin Sun,Ching Fei Li,Yu Han Wang,Yu Han Wang,Jun Yao,Hui Li,Hui Li,Meisi Yan,Meisi Yan,Wei Chao Chang,Jung Mao Hsu,Jung Mao Hsu,Jong Ho Cha,Jong Ho Cha,Jennifer L. Hsu,Cheng Wei Chou,Cheng Wei Chou,Xian Sun,Xian Sun,Yalan Deng,Chao Kai Chou,Dihua Yu,Mien Chie Hung,Mien Chie Hung +25 more
TL;DR: This paper showed that anti-Galectin-9 therapy selectively expands intratumoral TIM-3+ cytotoxic CD8 T cells and immunosuppressive regulatory T cells (Treg cells) and suggests Gal-9 as a promising target for immunotherapy.
Journal ArticleDOI
Galectin-3 negatively regulates TCR-mediated CD4+ T-cell activation at the immunological synapse
Huan Yuan Chen,Agnes Fermin,Santosh Vardhana,I-Chun Weng,Kin Fong Robin Lo,En-Yuh Chang,Emanual Michael Maverakis,Emanual Michael Maverakis,Ri Yao Yang,Daniel K. Hsu,Michael L. Dustin,Fu-Tong Liu +11 more
TL;DR: Galectin-3 was recruited to the cytoplasmic side of the immunological synapse (IS) in activated T cells as discussed by the authors and was associated with lower levels of early signaling events and phosphotyrosine signals at the pSMAC.
Journal ArticleDOI
Cell cycle regulation by galectin-12, a new member of the galectin superfamily.
TL;DR: It is concluded that galectin-12 is a novel regulator of cellular homeostasis, which contains two domains that are homologous to the galECTin CRD.
Journal ArticleDOI
Galectin-1 induces nuclear translocation of endonuclease G in caspase- and cytochrome c-independent T cell death
Hejin P. Hahn,Mabel Pang,Jiale He,Joseph D. Hernandez,Ri Yao Yang,Lily Y. Li,Xiaodong Wang,Fu-Tong Liu,Linda G. Baum +8 more
TL;DR: It is found that galectin-1 binding to human T cell lines triggered rapid translocation of endonuclease G from mitochondria to nuclei, however, endonUClease G nuclear translocation occurred without cytochrome c release from mitochondia, without nuclear translocated of apoptosis-inducing factor, and prior to loss of mitochondrial membrane potential.
Journal ArticleDOI
Galectins in acute and chronic inflammation
TL;DR: Galectins are animal lectins that bind to β‐galactosides, such as lactose and N‐acetyllactosamine, in free form or contained in glycoproteins or glycolipids, and can form lattices with membrane glycoprotein receptors and modulate receptor properties.